[HTML][HTML] Visualizing and trapping transient oligomers in amyloid assembly pathways

EE Cawood, TK Karamanos, AJ Wilson… - Biophysical chemistry, 2021 - Elsevier
Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

M Zhou, C Lantz, KA Brown, Y Ge, L Paša-Tolić… - Chemical …, 2020 - pubs.rsc.org
In biology, it can be argued that if the genome contains the script for a cell's life cycle, then
the proteome constitutes an ensemble cast of actors that brings these instructions to life …

Large scale relative protein ligand binding affinities using non-equilibrium alchemy

V Gapsys, L Pérez-Benito, M Aldeghi, D Seeliger… - Chemical …, 2020 - pubs.rsc.org
Ligand binding affinity calculations based on molecular dynamics (MD) simulations and non-
physical (alchemical) thermodynamic cycles have shown great promise for structure-based …

Biomolecular and biological applications of solid-state NMR with dynamic nuclear polarization enhancement

WY Chow, G De Paëpe, S Hediger - Chemical Reviews, 2022 - ACS Publications
Solid-state NMR spectroscopy (ssNMR) with magic-angle spinning (MAS) enables the
investigation of biological systems within their native context, such as lipid membranes, viral …

Molecular mechanisms of cardiac amyloidosis

Y Saito, K Nakamura, H Ito - International journal of molecular sciences, 2021 - mdpi.com
Cardiac involvement has a profound effect on the prognosis of patients with systemic
amyloidosis. Therapeutic methods for suppressing the production of causative proteins have …

Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid

LD Aubrey, N Ninkina, SM Ulamec… - Proceedings of the …, 2024 - National Acad Sciences
α-, β-, and γ-Synuclein are intrinsically disordered proteins implicated in physiological
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …

Structural basis for transthyretin amyloid formation in vitreous body of the eye

I Iakovleva, M Hall, M Oelker, L Sandblad… - Nature …, 2021 - nature.com
Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of
ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly …

Hereditary transthyretin amyloidosis overview

F Manganelli, GM Fabrizi, M Luigetti, P Mandich… - Neurological …, 2020 - Springer
Hereditary amyloidogenic transthyretin (ATTRv) amyloidosis is a rare autosomal dominantly
inherited disorder caused by mutations in the transthyretin (TTR) gene. The pathogenetic …

Fatty acids reverse the supramolecular chirality of insulin fibrils

AP Holman, K Quinn, R Kumar, S Kmiecik… - The Journal of …, 2023 - ACS Publications
Long-chain unsaturated and polyunsaturated fatty acids (LCUFAs and LCPUFAs,
respectively) are the essential components of phospholipids and sphingolipids, major …

Role of saturation and length of fatty acids of phosphatidylserine in the aggregation of transthyretin

A Ali, K Zhaliazka, T Dou, AP Holman… - ACS Chemical …, 2023 - ACS Publications
The progressive accumulation of transthyretin (TTR), a small protein that transports
thyroxine, in various organs and tissues is observed upon transthyretin amyloidosis, a …